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7-carboxy-7-deazaguanine synthase (CDG synthase) (EC 4.3.99.3) (Queuosine biosynthesis protein QueE)

 A0A071MD27_9ENTR        Unreviewed;       223 AA.
A0A071MD27;
01-OCT-2014, integrated into UniProtKB/TrEMBL.
01-OCT-2014, sequence version 1.
25-OCT-2017, entry version 19.
RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917};
Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917};
EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917};
AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917};
Name=queE {ECO:0000256|HAMAP-Rule:MF_00917};
ORFNames=DT73_00725 {ECO:0000313|EMBL:KEA54431.1};
Mangrovibacter sp. MFB070.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Mangrovibacter.
NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA54431.1, ECO:0000313|Proteomes:UP000027726};
[1] {ECO:0000313|EMBL:KEA54431.1, ECO:0000313|Proteomes:UP000027726}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MFB070 {ECO:0000313|EMBL:KEA54431.1,
ECO:0000313|Proteomes:UP000027726};
Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M.,
Lalitha K.V.;
"Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
Bacterium Isolated from an Aquaculture Farm.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated
conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-
carboxy-7-deazaguanine (CDG), a step common to the biosynthetic
pathways of all 7-deazapurine-containing compounds.
{ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7-
carboxy-7-carbaguanine + NH(3). {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
-!- COFACTOR:
Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
Note=Binds 1 S-adenosyl-L-methionine per subunit.
{ECO:0000256|HAMAP-Rule:MF_00917};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_00917};
-!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00917}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
deazaguanine synthase family. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00917}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEA54431.1}.
-----------------------------------------------------------------------
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EMBL; JJMI01000002; KEA54431.1; -; Genomic_DNA.
RefSeq; WP_036102883.1; NZ_JJMI01000002.1.
EnsemblBacteria; KEA54431; KEA54431; DT73_00725.
UniPathway; UPA00391; -.
Proteomes; UP000027726; Unassembled WGS sequence.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00917; QueE; 1.
InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR007197; rSAM.
InterPro; IPR027609; rSAM_QueE_Proteobac.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF000370; QueE; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
TIGRFAMs; TIGR04322; rSAM_QueE_Ecoli; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00917};
Complete proteome {ECO:0000313|Proteomes:UP000027726};
Iron {ECO:0000256|HAMAP-Rule:MF_00917};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00917};
Lyase {ECO:0000256|HAMAP-Rule:MF_00917};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00917};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00917};
Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917};
Reference proteome {ECO:0000313|Proteomes:UP000027726};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00917}.
DOMAIN 27 137 Radical_SAM. {ECO:0000259|Pfam:PF04055}.
REGION 12 14 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00917}.
REGION 37 39 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
REGION 136 138 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 31 31 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 35 35 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_00917}.
METAL 40 40 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 27 27 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 92 92 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00917}.
BINDING 94 94 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00917}.
SEQUENCE 223 AA; 24962 MW; CD4C092529B30C54 CRC64;
MQYPINEIFQ TLQGEGYFTG VPAIFIRLQG CPVGCAWCDT KHTWDKLAER EVSLFSVMAK
TKESDKWAAS TPEELLAVAN RQGYTARHVV ITGGEPCIHD LTPLTQLLEQ HGYQCQIETS
GTHEVLATAN TWVTVSPKVN MRGGYDVLGQ ALVRADEIKH PVGRVRDIEA LDALLATLSD
EKPRIIALQP ISQKEDATRL CIETCIERNW RLSMQTHKYL NIA


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